Purification and Activity of the Second Recombinant Enzyme for Biodegrading Linearized Microcystins by <i>Sphingopyxis</i> sp. USTB-05

Junhui Teng; Meijie Song; Qianqian Xu; Qianwen Zou; Haiyang Zhang; Chunhua Yin; Xiaolu Liu; Yang Liu; Hai Yan

doi:10.3390/toxins15080494

Toxins (Aug 2023)

Purification and Activity of the Second Recombinant Enzyme for Biodegrading Linearized Microcystins by <i>Sphingopyxis</i> sp. USTB-05

Junhui Teng,
Meijie Song,
Qianqian Xu,
Qianwen Zou,
Haiyang Zhang,
Chunhua Yin,
Xiaolu Liu,
Yang Liu,
Hai Yan

Affiliations

Junhui Teng: School of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China
Meijie Song: School of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China
Qianqian Xu: School of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China
Qianwen Zou: School of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China
Haiyang Zhang: School of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China
Chunhua Yin: School of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China
Xiaolu Liu: School of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China
Yang Liu: School of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China
Hai Yan: School of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China

DOI: https://doi.org/10.3390/toxins15080494
Journal volume & issue: Vol. 15, no. 8
p. 494

Abstract

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Hepatotoxic microcystins (MCs) are produced and released by the harmful bloom-forming cyanobacteria, which severely threaten drinking water safety and human health due to their high toxicity, widespread distribution, and structural stability. The linearized microcystinase (MlrB) further hydrolyses the poisonous linearized MCs produced by the microcystinase-catalysed MCs to form tetrapeptides. Here, the purification and activity of MlrB were investigated. The results showed that the linearized products generated by 12.5 mg/L MC-LR and MC-RR were removed by purified recombinant MlrB at a protein concentration of 1 mg/L within 30 min. The high catalytic activity of MlrB can be obtained via heterologous expression and affinity purification, which lays the foundation for further studies on the properties and mechanism of MCs biodegradation enzymes.

Published in Toxins

ISSN: 2072-6651 (Online)
Publisher: MDPI AG
Country of publisher: Switzerland
LCC subjects: Medicine
Website: http://www.mdpi.com/journal/toxins/

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